ProjectSummary-??FunctionalLnFe-??NxHyModelsofBiologicalN2Fixation Nitrogenase (N2ase) is a metalloenzyme that mediates biological nitrogen fixation and is essential to life. As such, the study of nitrogenase attracts intense scrutiny among the biology and chemistry communities. Nonetheless, the mechanism by which nitrogenase enzymes promote the biological reduction of nitrogen under ambient conditions remains a fascinating and unsolved problem. The broad goal of our research is to evaluate the mechanisms by which a single iron site is able to mediate catalytic N2 reduction in synthetic model systems and, by extension, in biology. The proposed program is to design and study biomimetic Fe-?? NxHy model complexes to address this goal. Our experimental approach stresses functionally, rather than structurally, faithful models of the iron-??molybdenum cofactor (FeMoco). Low molecular weight Fe-??NxHy complexes will be developed to explore iron sites in low coordinate geometries that may accommodate dinitrogen and other NxHy functionalities. We posit these geometries as relevant to Fe-??NxHy intermediates of the FeMoco. By analogy to the modes of Fe-??mediated biocatalytic O2 reduction, two limiting single-??site mechanisms are emphasized. The first is an alternating mechanism, where successive H-??atom transfers (via H+/e-??steps)occuratthedistalandproximalN-??atomsoftheFe-??N?Nsubunitinanalternatingfashion(e.g.,Fe-?? N=NH ? Fe-??NH=NH ? Fe-??NH-??NH2? Fe-??NH2-??NH2? Fe-??NH2 + NH3). The second is a distal mechanism, where complete H-??atom transfer at the distal N-??atom to liberate an NH3 equivalent precedes transfers to the proximalN-??atom(e.g.,Fe-??N2+3e-??+3H+?Fe?N+NH3).Wealsoexploreanewhybridmechanismthatfirst invokes a distal intermediate (Fe=NNH2) that then crosses to an alternating intermediate (Fe-??N2H4) before releasingthefirstNH3equivalent.Wewillusesyntheticmodelcomplexestotesttheviabilityofeachofthese mechanistic pathways, and to understand how the nuclearity, local geometry, and electronic structure of Fe-?? NxHy species control their relative stabilities and reactivity patterns. This knowledge will be applied to the study, via spectroscopic, electrochemical, and theoretical methods, of the first examples of single-??site iron catalystsforN2-??to-??NH3conversionthatwediscoveredinthepreviousgrantperiod,andtowardsthedesignof newN2-??fixingcatalystswithenhancedefficiency.Regardlessoftheprecisemechanismfornitrogenreduction attheFeMoco,itsultimatesolutionwillrequirecomparisonofspectroscopicdatafromthecofactortorelated data obtained for well-??defined model complexes. We will therefore continue to collaborate with researchers thatspecializeinspectroscopicstudiesoftheFeMocotomakesuchcomparisons,andotherinvestigatorswith expertisecomplementarytoourown.Insum,thefunctionalFe-??NxHymodelchemistryproposedwillcontinue to play a critical role alongside current biochemical, spectroscopic, and theoretical model studies aimed at unravelingthechemicalmechanismofbiologicalnitrogenfixation.